BIOMAT Database Logo BIOMAT Database Logo

Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcbeta 1-6(GlcNAcbeta 1-2)- manalpha 1-R[GlcNAc to man]beta 1,4N-acetylglucosaminyltransferase VI. 2000

Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Departments of Biochemistry and Ophthalmology, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

A cDNA that encodes UDP-N-acetyl-d-glucosamine (GlcNAc):GlcNAcbeta1-6(GlcNAcbeta1-2)Manalpha1-R[GlcNA c to Man]beta1, 4N-acetylglucosaminyltransferase VI (GnT VI), which is responsible for the formation of pentaantennary asparagine-linked oligosaccharides (N-glycans), has been cloned from a hen oviduct cDNA library based on the partial amino acid sequences of the purified enzyme. The isolated cDNA clone contained an open reading frame encoding 464 amino acids, including all of the peptides that were sequenced. The deduced amino acid sequence predicts a type II transmembrane topology and contains two potential N-glycosylation sites. The primary structure was found to be significantly similar to human GnT IV-homologue, the gene for which was cloned from the deleted region in pancreatic cancer, and to human and bovine GnT IVs. Chicken GnT VI-transfected COS-1 cells showed a high GnT VI activity (26.8 pmol/h/mg protein), whereas nontransfected, mock-transfected, or human GnT IV-homologue-transfected COS-1 cells had no activity. Northern blot analysis using poly(A)(+) RNA from hen oviduct indicated that the size of GnT VI mRNA is 2.1 kilobases. Reverse transcription-polymerase chain reaction analysis showed that GnT VI mRNA was relatively highly expressed in oviduct, spleen, lung, and colon.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010057 Oviducts Ducts that serve exclusively for the passage of eggs from the ovaries to the exterior of the body. In non-mammals, they are termed oviducts. In mammals, they are highly specialized and known as FALLOPIAN TUBES. Oviduct
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D005260 Female Females
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4N-acetylglucosaminyltransferase III from rat kidney.
September 1992, The Journal of biological chemistry,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Molecular cloning and expression of cDNA encoding the rat UDP-N-acetylglucosamine:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II.
June 1995, The Journal of biological chemistry,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Activity of UDP-GlcNAc:GlcNAc beta 1-->6(GlcNAc beta 1-->2) Man alpha 1-->R[GlcNAc to Man] beta 1-->4N-acetylglucosaminyltransferase VI (GnT VI) from the ovaries of Oryzias latipes (Medaka fish).
January 1997, Biochemical and biophysical research communications,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc beta 1-6 (GlcNAc beta 1-2)Man alpha-R (GlcNAc to Man) beta-4-N-acetylglucosaminyltransferase VI.
July 1989, The Journal of biological chemistry,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Mucin synthesis. UDP-GlcNAc:GalNAc-R beta 3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc beta 1-3GalNAc-R (GlcNAc to GalNAc) beta 6-N-acetylglucosaminyltransferase from pig and rat colon mucosa.
April 1985, Biochemistry,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
A method for determination of UDP-GlcNAc: GlcNAcβ1-6(GlcNAcβ1-2)Manα1-R [GlcNAc to Man] β1-4N-acetylglucosaminyltransferase VI activity.
January 2013, Methods in molecular biology (Clifton, N.J.),
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
UDP-GlcNAc: Gal beta 3GalNAc-mucin: (GlcNAc----GalNAc) beta 6-N-acetylglucosaminyltransferase and UDP-GlcNAc: Gal beta 3(GlcNAc beta 6) GalNAc-mucin (GlcNAc----Gal)beta 3-N-acetylglucosaminyltransferase from swine trachea epithelium.
March 1991, Molecular and cellular biochemistry,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Control of glycoprotein synthesis. IX. A terminal Man alpha l-3Man beta 1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: alpha-D-mannoside (GlcNAc to Man alpha 1-3) beta 2-N-acetylglucosaminyltransferase I.
June 1984, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
Regulation of UDP-GlcNAc:Gal beta 1-3GalNAc-R beta 1-6-N-acetylglucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells.
March 1993, The Journal of biological chemistry,
Y Sakamoto, and T Taguchi, and K Honke, and H Korekane, and H Watanabe, and Y Tano, and N Dohmae, and K Takio, and A Horii, and N Taniguchi
A coupled assay for UDP-GlcNAc:Gal beta 1-3GalNAc-R beta 1,6-N-acetylglucosaminyltransferase (GlcNAc to GalNAc).
November 1992, Analytical biochemistry,
Copied contents to your clipboard!